Publication: Characterization of short monomeric polyglutamine peptides by replica exchange molecular dynamics simulation
All || By Area || By Year| Title | Characterization of short monomeric polyglutamine peptides by replica exchange molecular dynamics simulation | Authors/Editors* | M. Nakano, H. Watanabe, S.M. Rothstein, and S. Tanaka |
|---|---|
| Where published* | J. Phys. Chem. B |
| How published* | Journal |
| Year* | 2010 |
| Volume | 114 |
| Number | |
| Pages | 7056-7061; 10234 |
| Publisher | |
| Keywords | |
| Link | |
| Abstract |
Polyglutamine (polyQ) diseases are caused by an abnormal expansion of CAG repeats. While their detailed structure remains unclear, polyQ peptides assume β-sheet structures when they aggregate. To investigate the conformational ensemble of short, monomeric polyQ peptides, which consist of 15 glutamine residues (Q15), we performed replica exchange molecular dynamics (REMD) simulations. We found that Q15 can assume multiple configurations due to all of the residues affecting the formation of side-chain hydrogen bonds. Analysis of the free energy landscape reveals that Q15 has a basin for random-coil structures and another for α-helix or β-turn structures. To investigate properties of aggregated polyQ peptides, we performed multiple molecular dynamics (MMD) simulations for monomeric and oligomeric Q15. MMD revealed that the formation of oligomers stabilizes the β-turn structure by increasing the number of hydrogen bonds between the main chains. |
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